Epstein-Barr virus (EBV) is the etiologic agent of infectious mononucleosis (IM), a co-factor in nasopharyngeal carcinoma and certain forms of B, NK and T cell lymphomas, and the root cause of B-cell lymphoproliferative disease in individuals with weakened immune systems. Although ubiquitous worldwide, nearly 50% of young adults and children in developed countries are susceptible to primary EBV infection and debilitating IM. An important clinical consequence of primary EBV infection in immunosuppressed transplant patients is post-transplant lymphoproliferative disorder (PTLD). The relative hazard for PTLD is 4- to 6-fold higher in organ recipients who were EBV seronegative prior to transplant compared to organ recipients who were EBV seropositive.
The EBV major virion surface glycoprotein (gp)350 is the principal target of naturally-occurring neutralizing antibodies and is viewed as the best vaccine candidate to prevent IM in healthy EBV-naive young adults or to prevent PTLD in at-risk organ recipients. Antibodies reactive to a single epitope on the 350 kDa virion surface glycoprotein (gp)350 block virus infection in vitro and prevent B cell lymphoma in primates.
There is thus a need for a better understanding of the core peptide sequence recognized by the 72A1 monoclonal antibody to allow for the design of a peptide vaccine that focuses the humoral immune system to this epitope.
The present description refers to a number of documents, the content of which is herein incorporated by reference in their entirety.